Evidence map›Paper›PMID 16093350›Full record

ArticleMolecular biology of the cell2005

Synaptotagmin isoforms couple distinct ranges of Ca2+, Ba2+, and Sr2+ concentration to SNARE-mediated membrane fusion.

Akhil Bhalla, Ward C Tucker, Edwin R Chapman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

93 citing papers in PubMed, 145 citations in OpenAlex.

  1. Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Different states of synaptic vesicle priming explain target cell type-dependent differences in neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Phospholipids Differentially Regulate CaACS chemical biology · 2024
    Article
  10. Complexin has a dual synaptic function as checkpoint protein in vesicle priming and as a promoter of vesicle fusion.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  15. Synaptotagmin 9 Modulates Spontaneous Neurotransmitter Release in Striatal Neurons by Regulating Substance P Secretion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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  16. Review
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  18. Synaptic Integration of Subquantal Neurotransmission by Colocalized G Protein-Coupled Receptors in Presynaptic Terminals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  19. Synaptotagmin 1 oligomerization via the juxtamembrane linker regulates spontaneous and evoked neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  20. Article

33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Akhil BhallaDepartment of Physiology, University of Wisconsin, Madison, WI 53706, USA.
Ward C Tucker
Edwin R Chapman
University of Wisconsin–Madison · US

Funding

Synaptotagmin C2B Domain as a Ca2+ Sensing ModuleR01MH061876 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI Edwin R Chapman · 2002 to 2026
$7.7M
SYNAPTOTAGMIN IN EXCITATION/SECRETION COUPLINGR01GM056827 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHAPMAN, EDWIN R · 1998 to 2006
$1.8M
NIGMS NIH HHS GM-56827NIGMS NIH HHS R01 GM056827NIMH NIH HHS MH-61876NIMH NIH HHS R01 MH061876
6 · The paper itself

Abstract

Ca2+-triggered exocytosis of synaptic vesicles is controlled by the Ca2+-binding protein synaptotagmin (syt) I. Fifteen additional isoforms of syt have been identified. Here, we compared the abilities of three syt isoforms (I, VII, and IX) to regulate soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-mediated membrane fusion in vitro in response to divalent cations. We found that different isoforms of syt couple distinct ranges of Ca2+, Ba2+, and Sr2+ to membrane fusion; syt VII was approximately 400-fold more sensitive to Ca2+ than was syt I. Omission of phosphatidylserine (PS) from both populations of liposomes completely abrogated the ability of all three isoforms of syt to stimulate fusion. Mutations that selectively inhibit syt.target-SNARE (t-SNARE) interactions reduced syt stimulation of fusion. Using Sr2+ and Ba2+, we found that binding of syt to PS and t-SNAREs can be dissociated from activation of fusion, uncovering posteffector-binding functions for syt. Our data demonstrate that different syt isoforms are specialized to sense different ranges of divalent cations and that PS is an essential effector of Ca2+.syt action.

Indexed as

AnimalsBariumCalciumCations, DivalentEthylmaleimideHumansIn Vitro TechniquesLiposomesMembrane FusionPhosphatidylserinesProtein BindingProtein IsoformsRatsSNARE ProteinsStrontiumSynaptotagmin IBariumCalciumCations, DivalentEthylmaleimideLiposomesPhosphatidylserinesProtein IsoformsSNARE ProteinsStrontiumSynaptotagmin ISyt1 protein, rat

Identifiers

PMID16093350
PMCPMC1237081
OpenAlexW2172248769

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.